1tvc
From Proteopedia
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| - | [[Image:1tvc.gif|left|200px]]< | + | [[Image:1tvc.gif|left|200px]] |
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| - | '''FAD and NADH binding domain of methane monooxygenase reductase from Methylococcus capsulatus (Bath)''' | + | {{Structure |
| + | |PDB= 1tvc |SIZE=350|CAPTION= <scene name='initialview01'>1tvc</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=FDA:DIHYDROFLAVINE-ADENINE DINUCLEOTIDE'>FDA</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Methane_monooxygenase Methane monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.25 1.14.13.25] | ||
| + | |GENE= mmoC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=414 Methylococcus capsulatus]) | ||
| + | }} | ||
| + | |||
| + | '''FAD and NADH binding domain of methane monooxygenase reductase from Methylococcus capsulatus (Bath)''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1TVC is a [ | + | 1TVC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methylococcus_capsulatus Methylococcus capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TVC OCA]. |
==Reference== | ==Reference== | ||
| - | NMR structure of the flavin domain from soluble methane monooxygenase reductase from Methylococcus capsulatus (Bath)., Chatwood LL, Muller J, Gross JD, Wagner G, Lippard SJ, Biochemistry. 2004 Sep 28;43(38):11983-91. PMID:[http:// | + | NMR structure of the flavin domain from soluble methane monooxygenase reductase from Methylococcus capsulatus (Bath)., Chatwood LL, Muller J, Gross JD, Wagner G, Lippard SJ, Biochemistry. 2004 Sep 28;43(38):11983-91. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15379538 15379538] |
[[Category: Methane monooxygenase]] | [[Category: Methane monooxygenase]] | ||
[[Category: Methylococcus capsulatus]] | [[Category: Methylococcus capsulatus]] | ||
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[[Category: fad-binding; nadh-binding]] | [[Category: fad-binding; nadh-binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:23:39 2008'' |
Revision as of 12:23, 20 March 2008
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| Ligands: | |||||||
| Gene: | mmoC (Methylococcus capsulatus) | ||||||
| Activity: | Methane monooxygenase, with EC number 1.14.13.25 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
FAD and NADH binding domain of methane monooxygenase reductase from Methylococcus capsulatus (Bath)
Overview
Soluble methane monooxygenase (sMMO) catalyzes the hydroxylation of methane by dioxygen to methanol, the first step in carbon assimilation by methanotrophs. This multicomponent system transfers electrons from NADH through a reductase component to the non-heme diiron center in the hydroxylase where O(2) is activated. The reductase component comprises three distinct domains, a [2Fe-2S] ferredoxin domain along with FAD- and NADH-binding domains. We report the solution structure of the reduced 27.6 kDa FAD- and NADH-binding domains (MMOR-FAD) of the reductase from Methylococcus capsulatus (Bath). The FAD-binding domain consists of a six-stranded antiparallel beta-barrel and one alpha-helix, with the first 10 N-terminal residues unstructured. In the interface between the two domains, the FAD cofactor is tightly bound in an unprecedented extended conformation. The NADH-binding domain consists of a five-stranded parallel beta-sheet with four alpha-helices packing closely around this sheet. MMOR-FAD is structurally homologous to other FAD-containing oxidoreductases, and we expect similar structures for the FAD/NADH-binding domains of reductases that occur in other multicomponent monooxygenases.
About this Structure
1TVC is a Single protein structure of sequence from Methylococcus capsulatus. Full crystallographic information is available from OCA.
Reference
NMR structure of the flavin domain from soluble methane monooxygenase reductase from Methylococcus capsulatus (Bath)., Chatwood LL, Muller J, Gross JD, Wagner G, Lippard SJ, Biochemistry. 2004 Sep 28;43(38):11983-91. PMID:15379538
Page seeded by OCA on Thu Mar 20 14:23:39 2008
